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Translational Neuroscience

, Volume 4, Issue 4, pp 385–409 | Cite as

Modulators of amyloid protein aggregation and toxicity: EGCG and CLR01

  • Aida Attar
  • Farid Rahimi
  • Gal Bitan
Review Article

Abstract

Abnormal protein folding and self-assembly causes over 30 cureless human diseases for which no disease-modifying therapies are available. The common side to all these diseases is formation of aberrant toxic protein oligomers and amyloid fibrils. Both types of assemblies are drug targets, yet each presents major challenges to drug design, discovery, and development. In this review, we focus on two small molecules that inhibit formation of toxic amyloid protein assemblies — the green-tea derivative (−)-epigallocatechin-3-gallate (EGCG), which was identified through a combination of epidemiologic data and a compound library screen, and the molecular tweezer CLR01, whose inhibitory activity was discovered in our group based on rational reasoning, and subsequently confirmed experimentally. Both compounds act in a manner that is not specific to one particular protein and thus are useful against a multitude of amyloidogenic proteins, yet they act via distinct putative mechanisms. CLR01 disrupts protein aggregation through specific binding to lysine residues, whereas the mechanisms underlying the activity of EGCG are only recently beginning to unveil. We discuss current in vitro and, where available, in vivo literature related to EGCG and CLR01’s effects on amyloid β-protein, α-synuclein, transthyretin, islet amyloid polypeptide, and calcitonin. We also describe the toxicity, pharmacokinetics, and mechanism of action of each compound.

Keywords

Amyloid Amyloidosis Alzheimer’s disease Parkinson’s disease Inhibitor Molecular tweezers Polyphenol 

Abbreviations

ADAD

Alzheimer’s disease

AFM

Atomic force microscopy

Amyloid beta

APP

Amyloid β-protein precursor

COMT

Catechol-O-methyltransferase

CYP 450

Cytochrome P450

EC

Epicatechin

ECG

Epicatechin-3-gallate

EGC

Epigallocatechin

EGCG

Epigallocatechin-3-gallate

EM

Electron microscopy

FAP

Familial amyloidotic polyneuropathy

IAPP

Islet amyloid polypeptide

IC50

Half maximal inhibitory concentration

IP

Intraperitoneal

MPTP

1 - Methyl-4-phenyl-1, 2, 3, 6-tetrahydropyridine

MT

Molecular tweezer

MTT

3-(4,5-Dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide

NBT

Nitroblue-tetrazolium

NMR

Nuclear magnetic resonance

PD

Parkinson’s disease

SDS-PAGE

Sodium dodecyl sulfate polyacrylamide gel electrophoresis

SPRi

Surface plasmon resonance imaging

ThT

Thioflavin T

TTR

Transthyretin

UPS

Ubiquitin-proteasome system

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Copyright information

© Versita Warsaw and Springer-Verlag Wien 2013

Authors and Affiliations

  1. 1.Department of Neurology, David Geffen School of MedicineUniversity of California at Los AngelesLos AngelesUSA
  2. 2.Brain Research InstituteUniversity of California at Los AngelesLos AngelesUSA
  3. 3.Molecular Biology InstituteUniversity of California at Los AngelesLos AngelesUSA
  4. 4.Research School of Biology, College of Medicine, Biology, and EnvironmentThe Australian National UniversityCanberraAustralia

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